Dynamics of SARS-CoV-2 spike protein in open and closed states and identification of key structural perturbations upon mutations

The SARS-Cov-2 spike protein resides on the exterior surface of the coronavirus, and therefore, acts as the first point of contact that mediates cell attachment and fusion.  During this process, it undergoes dramatic conformational changes upon host receptor binding. We are leveraging high-performance computing to identify these structural perturbations in wildtype and mutant spike protein models. The files contain structures from molecular dynamics simulations of closed SARS-Cov-2 spike protein embedded in POPC membrane.